The dapE-encoded N-Succinyl-l,l-Diaminopimelic Acid Desuccinylase from Haemophilus influenzae Is a Dinuclear MetallohydrolaseJournal of the American Chemical Society
Format of Original2 p.
PublisherAmerican Chemical Society
Original Item IDDOI: 10.1021/ja036650v
AbstractThe Zn K-edge extended X-ray absorption fine structure (EXAFS) spectra, of the dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase (DapE) from Haemophilus influenzae have been recorded in the presence of one or two equivalents of Zn(II) (i.e. [Zn_(DapE)] and [ZnZn(DapE)]). The Fourier transforms of the Zn EXAFS are dominated by a peak at ca. 2.0 Å, which can be fit for both [Zn_(DapE)] and [ZnZn(DapE)], assuming ca. 5 (N,O) scatterers at 1.96 and 1.98 Å, respectively. A second-shell feature at ca. 3.34 Å appears in the [ZnZn(DapE)] EXAFS spectrum but is significantly diminished in [Zn_(DapE)]. These data show that DapE contains a dinuclear Zn(II) active site. Since no X-ray crystallographic data are available for any DapE enzyme, these data provide the first glimpse at the active site of DapE enzymes. In addition, the EXAFS data for DapE incubated with two competitive inhibitors, 2-carboxyethylphosphonic acid and 5-mercaptopentanoic acid, are also presented.
Citation InformationNathaniel J. Cosper, David L. Bienvenue, Jacob E. Shokes, Danuta M. Gilner, et al.. "The dapE-encoded N-Succinyl-l,l-Diaminopimelic Acid Desuccinylase from Haemophilus influenzae Is a Dinuclear Metallohydrolase" Journal of the American Chemical Society (2003) ISSN: 0002-7863
Available at: http://works.bepress.com/richard_holz/50/